A serine involved in actin-dependent subcellular localization of a stress-induced tobacco BY-2 hydroxymethylglutaryl-CoA reductase isoform
| العنوان: | A serine involved in actin-dependent subcellular localization of a stress-induced tobacco BY-2 hydroxymethylglutaryl-CoA reductase isoform |
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| المؤلفون: | Jean Roger Cirioni, Andréa Hemmerlin, Rémy Merret, Thomas J. Bach |
| المساهمون: | Institut de biologie moléculaire des plantes (IBMP), Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS) |
| المصدر: | FEBS Letters FEBS Letters, Wiley, 2007, 581, pp.5295-5299 |
| بيانات النشر: | Wiley, 2007. |
| سنة النشر: | 2007 |
| مصطلحات موضوعية: | 0106 biological sciences, Gene isoform, DNA, Plant, Calmodulin, Recombinant Fusion Proteins, Green Fluorescent Proteins, Molecular Sequence Data, Biophysics, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, Biology, Reductase, Endoplasmic Reticulum, 01 natural sciences, Biochemistry, Cell Line, Serine, 03 medical and health sciences, Structural Biology, Tobacco, Plant HMG-CoA reductase, Genetics, Amino Acid Sequence, Cloning, Molecular, Molecular Biology, Actin, 030304 developmental biology, 0303 health sciences, Base Sequence, Sequence Homology, Amino Acid, ER retention, Cell Biology, Plants, Genetically Modified, Subcellular localization, Actins, Protein Structure, Tertiary, Cell biology, Isoenzymes, Cytoplasm, Membrane domain, biology.protein, Hydroxymethylglutaryl CoA Reductases, Subcellular Fractions, 010606 plant biology & botany |
| الوصف: | 3-Hydroxy-3-methylglutaryl-CoA reductase (HMGR) is unique in the first part of the cytoplasmic isoprenoid pathway, as it contains a membrane domain that includes ER-specific retention motifs. When fused to GFP, this domain targets two tobacco BY-2 HMGR isoforms differentially. While the first isoform is ER-localized, a second stress-induced one forms globular structures connected by tubular structures. A serine positioned upstream of the ER retention motif seems to be implicated in this specific subcellular localization. Surprisingly, these structures are closely connected to F-actin, and their intactness is dependent upon the integrity of the filaments or the action of a calmodulin antagonist. |
| تدمد: | 0014-5793 1873-3468 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d14c1d6a76a864b15076ccb9aa675315 https://doi.org/10.1016/j.febslet.2007.10.023 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....d14c1d6a76a864b15076ccb9aa675315 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 00145793 18733468 |
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